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Biophysics
Index: #16

Some Proteins Are Still Recalcitrant to Experimental Structure Analysis

Membrane proteins are notoriously difficult to analyze experimentally and to incorporate into technological applications due to their inherent insolubility in aqueous environments. Their recalcitrance limits our capacity to study their structure and function in detail. Other challenges include the difficulty of studying small proteins with cryo-EM.

Foundational Capabilities (2)

Recode Membrane Proteins for Solubility

Modify the genetic code or structure of membrane proteins so they become soluble in water, thereby enabling more robust experimental analysis and practical applications.
  • Computational design of soluble and functional membrane protein analogues
    Technology Seed
  • Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code
    Technology Seed

    • Make it Easier to Map Orientations of Small Proteins in Cryo-Em

    Barcode the orientations of small proteins in the cryo-EM
  • Molecular goniometers for single-particle cryo-electron microscopy of DNA-binding proteins
    Technology Seed